Journal
JOURNAL OF NEUROSCIENCE
Volume 30, Issue 10, Pages 3728-3738Publisher
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.2024-09.2010
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Funding
- Fondo Nacional de Desarrollo Cientifico y Tecnologico [1040782, 1080221, 3070017]
- Fondo de Investigacion Avanzada en Areas Prioritarias - Biomedicine [13980001]
- Millennium Institute for Fundamental and Applied Biology
- Mejoramiento de la Calidad y la Equidad de la Educacion Superior-Pontificia Universidad Catolica de Chile [0780]
- National Institutes of Health [NS39475]
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The c-Abl tyrosine kinase is present in mouse brain synapses, but its precise synaptic function is unknown. We found that c-Abl levels in the rat hippocampus increase postnatally, with expression peaking at the first postnatal week. In 14 d in vitro hippocampal neuron cultures, c-Abl localizes primarily to the postsynaptic compartment, in which it colocalizes with the postsynaptic scaffold protein postsynaptic density protein-95 (PSD-95) in apposition to presynaptic markers. c-Abl associates with PSD-95, and chemical or genetic inhibition of c-Abl kinase activity reduces PSD-95 tyrosine phosphorylation, leading to reduced PSD-95 clustering and reduced synapses in treated neurons. c-Abl can phosphorylate PSD-95 on tyrosine 533, and mutation of this residue reduces the ability of PSD-95 to cluster at postsynaptic sites. Our results indicate that c-Abl regulates synapse formation by mediating tyrosine phosphorylation and clustering of PSD-95.
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